In silico prediction of the binding structure between vitellogenin and vitellogenin receptor of Haemaphysalis longicornis.

Authors

Meryem Behri, Hayato Kawada, Yuki Koike, Sana Sasaki, Kofi Dadzie Kwofie, Hanako Kunisada, Takahiro Inoue, Keiko Mizutani, Kei Jimbo, Fusako Mikami, Kiyomasa Machida, Makoto Matsubayashi, Naotoshi Tsuji, Takeshi Hatta, Yasunobu Matsumoto

Published in

The Journal of veterinary medical science. Sep 29, 2025. Epub Sep 29, 2025.

Abstract

Vitellogenin (Vtg) and its receptor (VtgR)-essential for yolk deposition and transovarial pathogen transmission in ticks-are compelling targets for antibody-based intervention. To investigate their interaction in the tick Haemaphysalic longicornis, we employed AlphaFold2 to model the β-barrel domain of the midgut-synthesized paralog HlVtg1 and the first three ligand-binding repeats (LBR1-3) of HlVtgR. Subsequent protein-protein docking in Molecular Operating Environment (MOE) revealed a recurrent binding interface centered on HlVtg1's Glu87, which formed persistent electrostatic interactions with LBR1-3 across top-ranking poses. Our results support a "monomeric engagement" model, where a single HlVtg1 monomer simultaneously engages all three low-density lipoprotein receptor class-A (LDLRA) domains of HlVtgR. This mechanism contrasts with the classical dimeric model and challenges prior inferences about stoichiometry and symmetry of binding sites. The predicted contact residues defined here may serve as a useful basis for evaluating candidate epitopes for interventions aimed at disrupting oocyte maturation and transovarial transmission of pathogens in H. longicornis.

PMID:
41016752
Bibliographic data and abstract were imported from PubMed on 29 Sep 2025.

Read full publication at:
Please sign in to see all details.

Stats

1-terrible, 9-excellent. How would you rate this publication? Sign in in to submit your rating.

Post a comment

You need to be signed in to post comments. You can sign in here.

Comments

There are no comments yet.